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Rockefeller University Press, Journal of Cell Biology, 5(148), p. 925-930, 2000

DOI: 10.1083/jcb.148.5.925

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The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum–Derived Vesicles

Journal article published in 2000 by Manuel Muñiz, Claude Nuoffer, Hans-Peter Hauri, Howard Riezman ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Members of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex required for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The specific functions and sites of action of this complex are unknown. We show that Emp24p is directly required for efficient packaging of a lumenal cargo protein, Gas1p, into ER-derived vesicles. Emp24p and Erv25p can be directly cross-linked to Gas1p in ER-derived vesicles. Gap1p, which was not affected by emp24 mutation, was not cross-linked. These results suggest that the Emp24 complex acts as a cargo receptor in vesicle biogenesis from the ER.